Structural confidence and template coverage of selected proteins from Flavobacterium azizsancarii

The Antarctic bacterium Flavobacterium azizsancarii provides a public genomic resource for investigating microbial enzyme diversity, but structural confidence does not establish the biochemical functions of individual proteins. This study examined 25 annotated proteins selected from the draft genome of strain AC, including ten candidates associated with phosphorus or carbohydrate metabolism. Coding sequences were verified against both the genome and corresponding RefSeq protein records. Five AlphaFold Server diffusion samples were analysed for each protein, giving 125 predicted structures. Residue confidence, predicted aligned error, coordinate agreement and archived template mappings were evaluated together. Median protein-level mean alpha-carbon confidence was 95.19, and 23 of 25 representative models had means of at least 90. Median predicted template modelling score was 0.94. The median global alpha-carbon root mean square deviation across 250 within-protein sample pairs was 0.54 Å, falling to 0.16 Å after independently aligning positions with confidence of at least 70 in both samples. A 1146-residue mutase-family protein contained confidently modelled cobalamin-binding, guanosine triphosphatase and mutase regions. Archived mappings to the known isobutyryl-coenzyme A mutase fusion structure 4XC6 covered 93.37% of its sequence at 60.65% identity, supporting a template-informed family assignment. A helicase and an FK506-binding peptidyl-prolyl isomerase showed greater regional uncertainty despite confident local segments. The analysis identifies tractable structural hypotheses without establishing new folds, substrate specificity or environmental performance.